Abstract
Isolation of antigen-specific lymphocyte receptors can be achieved by high-performance immunoaffinity chromatography, using immobilized monoclonal anti-bodies directed against the antigen. Primed lymphocytes are allowed to react with their target antigen prior to disruption and membrane solubilization. The bound antigen acts both as a preservative for the receptor and as a ligand on which the immobilized antibody captures the antigen-receptor complex. Dissociation of the antigen-antibody complex also releases the antigen from the receptor, and both antigen and receptor can be separated and recovered for further study.
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